We are analyzing https://link.springer.com/article/10.1007/bf00036962.

Title:
Common amino acid sequence domains among the LEA proteins of higher plants | Plant Molecular Biology
Description:
LEA proteins are late embryogenesis abundant in the seeds of many higher plants and are probably universal in occurrence in plant seeds. LEA mRNAs and proteins can be induced to appear at other stages in the plant
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Keywords {🔍}

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Topics {✒️}

tuan-hua david ho month download article/chapter abscisic acid-inducible mrna plant molecular biology amino acid sequence abscisic acid induction late embryogenesis abundant vivo protein synthesis represent protein structures privacy choices/manage cookies wheat em protein protecting plant structures full article pdf representative plant species stress transduction process higher plants published abscisic acid water stress induce european economic area found tandemly repeated pattern recognition receptors barley aleurone layers de novo design flanking peptide bonds lea family members conditions privacy policy desiccation stress mrna rapidly induced article dure amphiphilic α helix helical net-diagrams molecular basis plant embryogenesis abiotic stress accepting optional cookies cdna clone encoding unusual sequence nucleotide sequence genes developmentally regulated main content log higher order structure check access instant access journal finder publish desiccation protection plant pathology sung rights higher plants sung department plant seeds

Schema {🗺️}

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         headline:Common amino acid sequence domains among the LEA proteins of higher plants
         description:LEA proteins are late embryogenesis abundant in the seeds of many higher plants and are probably universal in occurrence in plant seeds. LEA mRNAs and proteins can be induced to appear at other stages in the plant's life by desiccation stress and/or treatment with the plant hormone abscisic acid (ABA). A role in protecting plant structures during water loss is likely for these proteins, with ABA functioning in the stress transduction process. Presented here are conserved tracts of amino acid sequence among LEA proteins from several species that may represent domains functionally important in desiccation protection. Curiously, an 11 amino acid sequence motif is found tandemly repeated in a group of LEA proteins of vastly different sizes. Analysis of this motif suggests that it exists as an amphiphilic α helix which may serve as the basis for higher order structure.
         datePublished:
         dateModified:
         pageStart:475
         pageEnd:486
         sameAs:https://doi.org/10.1007/BF00036962
         keywords:
            LEA protein sequence
            plant desiccation
            abscisic acid
            Plant Sciences
            Biochemistry
            general
            Plant Pathology
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      headline:Common amino acid sequence domains among the LEA proteins of higher plants
      description:LEA proteins are late embryogenesis abundant in the seeds of many higher plants and are probably universal in occurrence in plant seeds. LEA mRNAs and proteins can be induced to appear at other stages in the plant's life by desiccation stress and/or treatment with the plant hormone abscisic acid (ABA). A role in protecting plant structures during water loss is likely for these proteins, with ABA functioning in the stress transduction process. Presented here are conserved tracts of amino acid sequence among LEA proteins from several species that may represent domains functionally important in desiccation protection. Curiously, an 11 amino acid sequence motif is found tandemly repeated in a group of LEA proteins of vastly different sizes. Analysis of this motif suggests that it exists as an amphiphilic α helix which may serve as the basis for higher order structure.
      datePublished:
      dateModified:
      pageStart:475
      pageEnd:486
      sameAs:https://doi.org/10.1007/BF00036962
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         LEA protein sequence
         plant desiccation
         abscisic acid
         Plant Sciences
         Biochemistry
         general
         Plant Pathology
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         type:PostalAddress
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         type:PostalAddress
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         type:PostalAddress
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      affiliation:
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            address:
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               type:PostalAddress
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      name:Tuan-Hua David Ho
      affiliation:
            name:Washington University
            address:
               name:Biology Department, Washington University, St. Louis, USA
               type:PostalAddress
            type:Organization
      name:John Mundy
      affiliation:
            name:The Rockefeller University
            address:
               name:Laboratory of Plant Molecular Biology, The Rockefeller University, New York, USA
               type:PostalAddress
            type:Organization
      name:Ralph Quatrano
      affiliation:
            name:University of North Carolina
            address:
               name:Department of Biology, University of North Carolina, Chapel Nill, USA
               type:PostalAddress
            type:Organization
      name:Terry Thomas
      affiliation:
            name:Texas A & M University
            address:
               name:Department of Biology, Texas A & M University, College Station, USA
               type:PostalAddress
            type:Organization
      name:Z. R. Sung
      affiliation:
            name:University of California
            address:
               name:Department of Genetics, University of California, Berkeley, USA
               type:PostalAddress
            type:Organization
            name:University of California
            address:
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      name:Department of Botany, University of California, Davis, USA
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      name:Laboratory of Plant Molecular Biology, The Rockefeller University, New York, USA
      name:Department of Biology, University of North Carolina, Chapel Nill, USA
      name:Department of Biology, Texas A & M University, College Station, USA
      name:Department of Genetics, University of California, Berkeley, USA
      name:Department of Plant Pathology, University of California, Berkeley, USA
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